Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6KHC8

Entry ID Method Resolution Chain Position Source
AF-Q6KHC8-F1 Predicted AlphaFoldDB

No variants for Q6KHC8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6KHC8

No associated diseases with Q6KHC8

3 regional properties for Q6KHC8

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 97 - 343 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 27 - 92 IPR004188
domain Aminoacyl-tRNA synthetase, class II 114 - 334 IPR006195

Functions

Description
EC Number 6.1.1.20 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.
phenylalanine-tRNA ligase activity Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
tRNA binding Binding to a transfer RNA.

1 GO annotations of biological process

Name Definition
phenylalanyl-tRNA aminoacylation The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIFSYKHLKK LANLNEISFE DVIKAFNLIG FEVEETKEIR HVENIKYGKV LKIYKNENSD
70 80 90 100 110 120
NLTVCEIQFK DKIRIIQTTA KNVEINKYVM AFIPGSKLAN NLIESKLLKG IISEGMLVGF
130 140 150 160 170 180
DEMLGFEIKL VPKELSKNVI VLDEANLNED PIANLELHDY LIDLAILPNR SDAISYLVMA
190 200 210 220 230 240
KELAAFFGTK IDNDLICLKN LRVSKINSNL EGIFVKSKTL ELKLYDKYLL LKSHLKLTNT
250 260 270 280 290 300
YKDLENLILI HTGMPIHFLN LKSLEKVNIV SKSSSLEIAN RTLKIDNNLV IEKSREIIAI
310 320 330 340 350 360
PYLETQKEFE IKDSQKEFFI FMNILSPKEV RKTIKTLKLE SSQIKQATKT ISHGMQLNAI
370 380 390 400 410 420
QYMQSLFEEI EIVNINLNLK PKEILFDHTF INRIAGFEIV KEQKFINAKK SLEILGFKFF
430 440 450 460 470 480
EDKILVPAYR HDYTGPYDVI EELFRFYGYD NFPILQPEIK PFKIQKKYDF KFSLASKNYN
490 500 510 520 530 540
EIKTYSLVAK EDNNFDPFNF KTEILMKTFP SEKRRIIRNS QAFSLLEIAE YNIKRKLEKI
550 560 570 580 590 600
NFFDFGMINE GKRALIFASN EKSFNEIKKD LFSLFSYKFE LRKTKNNYLH PNASAHIFYE
610 620 630 640 650 660
NKLIGWMGKI NPSLKISDLI FVEILLDEFN ISKNQFKEYN FDPLKFRDIT FSIEKNQSID
670 680 690 700 710
TYLKELKKIK NIFEVQIIDK FEKNEKLNIT VRILLEDDAI KNLDEAILKN SWN